2YPH
Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutation H230S, crystallized with 2',3-(RP)- cyclic-AMPS
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-2 |
| Synchrotron site | MAX II |
| Beamline | I911-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-02-02 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 40.630, 47.530, 107.550 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 26.887 - 2.100 |
| R-factor | 0.2329 |
| Rwork | 0.230 |
| R-free | 0.28880 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2xmi |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.502 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.000 | 2.150 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.090 | 0.840 |
| Number of reflections | 12336 | |
| <I/σ(I)> | 13.4 | 2 |
| Completeness [%] | 96.7 | 92.1 |
| Redundancy | 5.9 | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4 | 277 | 250 UM PROTEIN AND 10 MM 23-(RP)-CYCLIC AMPS WAS MIXED IN 0.5 PLUS 0.5 UL DROPS WITH 30% PEG4000 AND 50 MM ACETATE (2:1 PH 3 AND 5) IN 4C TEMP |
